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Supplier: SIGMA ALDRICH MICROSCOPY
Description: Immersion Oil has a defined refractive index of about 1,516. It is important that the refractive index (nD) is about 1,5, similar to that of glass. This enables a homogeneous oil immersion to be achieved.

Supplier: VWR Collection
Description: Dual-scale handheld refractometers designed to provide ranges of Brix (sugar concentration) and refractive index measurements.

Supplier: Apollo Scientific
Description: Affords low refractive index polymer.

Catalog Number: (C9368-30ML)
Supplier: SIGMA ALDRICH MICROSCOPY
Description: CC/mount is an aqueous based permanent mounting medium with a very high refractive index, which when applied to the stained tissue sections can store the tissue specimens permanently without the fading of the chromogens. Because of the superior refractive index of CC/mount, tissues mounted in this medium look like specimens mounted with organic based mounting media. No coverslipping is required with CC/mount. However, if coverslipping is required, dried CC/mount can be post mounted by using an organic based mounting medium. CC/mount permits the long-term storage of antigens localised using organic insoluble chromogen substrates, including AEC, DAB, Fast Red, BCIP/NBT, BCIP/INT and fluorescent dyes like FITC and phycobiliproteins. The high pH of CC/mount ensures increased stability of fluorescence intensity.
UOM: 1 * 30 mL


Catalog Number: (635-0480)
Supplier: BELLINGHAM STANLEY
Description: The Abbe refractometer is designed for applications in educational establishments and laboratories, where wide refractive index ranges are required, or where sample throughput is relatively low.
UOM: 1 * 1 items


Supplier: cphnano
Description: Get accurate quantification by upgrading a UV-Vis spectrophotometer with user-friendly cuvettes. The NanoCuvette™ One expands the capabilities of an UV/Vis spectrophotometer to include quantification via refractive index for QC, kinetics, and 0,5 μl sample measurements.

Catalog Number: (BOSSBS-13276R-FITC)
Supplier: Bioss
Description: Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into alpha, beta, and gamma families, and the beta and gamma-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. gamma-crystallins are structural proteins in the lens, and they exists as monomers which typically lack connecting peptides and terminal extensions. The gamma-crystallins include seven closely related gamma A, gamma B, gamma C, gamma D, gamma E, gamma F, and gamma G-crystallin, as well as the gamma N and gamma S-crystallin genes. The gamma-crystallins are differentially regulated after early development, and are involved in cataract formation as a result of either age-related protein degradation or genetic mutation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9585R-CY7)
Supplier: Bioss
Description: Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated α, β and γ. Crystallins, as the principal components of the lens, function to increase the refractive index of the eye during accommodation by forming high-molecular weight aggregates which maintain transparency. γS-crystallin (Gamma-crystallin S), also known as Beta-crystallin S, is a 178 amino acid protein that exists as a monomer which does not aggregate. γS-crystallin contains a two-domain beta structure and belongs to the beta/gamma-crystallin gene family mapping to human chromosome 3. γS-crystallin has been linked to congenital cataract development, a disorder signified by increasing levels of lens opacity.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9585R-A555)
Supplier: Bioss
Description: Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated α, β and γ. Crystallins, as the principal components of the lens, function to increase the refractive index of the eye during accommodation by forming high-molecular weight aggregates which maintain transparency. γS-crystallin (Gamma-crystallin S), also known as Beta-crystallin S, is a 178 amino acid protein that exists as a monomer which does not aggregate. γS-crystallin contains a two-domain beta structure and belongs to the beta/gamma-crystallin gene family mapping to human chromosome 3. γS-crystallin has been linked to congenital cataract development, a disorder signified by increasing levels of lens opacity.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9585R-A350)
Supplier: Bioss
Description: Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated α, β and γ. Crystallins, as the principal components of the lens, function to increase the refractive index of the eye during accommodation by forming high-molecular weight aggregates which maintain transparency. γS-crystallin (Gamma-crystallin S), also known as Beta-crystallin S, is a 178 amino acid protein that exists as a monomer which does not aggregate. γS-crystallin contains a two-domain beta structure and belongs to the beta/gamma-crystallin gene family mapping to human chromosome 3. γS-crystallin has been linked to congenital cataract development, a disorder signified by increasing levels of lens opacity.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9585R-HRP)
Supplier: Bioss
Description: Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated α, β and γ. Crystallins, as the principal components of the lens, function to increase the refractive index of the eye during accommodation by forming high-molecular weight aggregates which maintain transparency. γS-crystallin (Gamma-crystallin S), also known as Beta-crystallin S, is a 178 amino acid protein that exists as a monomer which does not aggregate. γS-crystallin contains a two-domain beta structure and belongs to the beta/gamma-crystallin gene family mapping to human chromosome 3. γS-crystallin has been linked to congenital cataract development, a disorder signified by increasing levels of lens opacity.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12859R-CY7)
Supplier: Bioss
Description: Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into a, b, and g families, and the b- and g-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. b-crystallins constitute the major lens structural proteins. They associate into dimers, tetramers, and higher order aggregates. The b-crystallin subfamily is composed of several gene products, including bA1-, bA2-, bA3-, bA4-, bB1-, bB2- and bB3-crystallin. The bA1- and bA3-crystallin proteins are encoded by a single mRNA. They differ by only 17 amino acids, and bA1-crystallin is generated by use of an alternate translation initiation site. The genes for bA4-, bB1-, bB2- and bB3-crystallin are clustered on human chromosome 22q11, while the genes for bA3/A1- and bA2-crystallin map to human chromosomes 17q11 and 2q34, respectively.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12859R-A680)
Supplier: Bioss
Description: Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into a, b, and g families, and the b- and g-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. b-crystallins constitute the major lens structural proteins. They associate into dimers, tetramers, and higher order aggregates. The b-crystallin subfamily is composed of several gene products, including bA1-, bA2-, bA3-, bA4-, bB1-, bB2- and bB3-crystallin. The bA1- and bA3-crystallin proteins are encoded by a single mRNA. They differ by only 17 amino acids, and bA1-crystallin is generated by use of an alternate translation initiation site. The genes for bA4-, bB1-, bB2- and bB3-crystallin are clustered on human chromosome 22q11, while the genes for bA3/A1- and bA2-crystallin map to human chromosomes 17q11 and 2q34, respectively.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12859R-HRP)
Supplier: Bioss
Description: Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into a, b, and g families, and the b- and g-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. b-crystallins constitute the major lens structural proteins. They associate into dimers, tetramers, and higher order aggregates. The b-crystallin subfamily is composed of several gene products, including bA1-, bA2-, bA3-, bA4-, bB1-, bB2- and bB3-crystallin. The bA1- and bA3-crystallin proteins are encoded by a single mRNA. They differ by only 17 amino acids, and bA1-crystallin is generated by use of an alternate translation initiation site. The genes for bA4-, bB1-, bB2- and bB3-crystallin are clustered on human chromosome 22q11, while the genes for bA3/A1- and bA2-crystallin map to human chromosomes 17q11 and 2q34, respectively.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12859R-FITC)
Supplier: Bioss
Description: Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into a, b, and g families, and the b- and g-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. b-crystallins constitute the major lens structural proteins. They associate into dimers, tetramers, and higher order aggregates. The b-crystallin subfamily is composed of several gene products, including bA1-, bA2-, bA3-, bA4-, bB1-, bB2- and bB3-crystallin. The bA1- and bA3-crystallin proteins are encoded by a single mRNA. They differ by only 17 amino acids, and bA1-crystallin is generated by use of an alternate translation initiation site. The genes for bA4-, bB1-, bB2- and bB3-crystallin are clustered on human chromosome 22q11, while the genes for bA3/A1- and bA2-crystallin map to human chromosomes 17q11 and 2q34, respectively.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9585R-A488)
Supplier: Bioss
Description: Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated α, β and γ. Crystallins, as the principal components of the lens, function to increase the refractive index of the eye during accommodation by forming high-molecular weight aggregates which maintain transparency. γS-crystallin (Gamma-crystallin S), also known as Beta-crystallin S, is a 178 amino acid protein that exists as a monomer which does not aggregate. γS-crystallin contains a two-domain beta structure and belongs to the beta/gamma-crystallin gene family mapping to human chromosome 3. γS-crystallin has been linked to congenital cataract development, a disorder signified by increasing levels of lens opacity.
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us at +43 1 97002 - 0.
Dual use goods can only be delivered within the European Union.
Dual use goods can only be delivered within the European Union.
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The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at +43 1 97002 - 0.
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